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Membrane protein structure determination remains a challenging endeavor.
In a Perspective, MacKinnon discusses the implications of this work for membrane protein structure and function.
Since the first eukaryotic membrane protein structure was determined in 2005, over sixty structures have been emerged until now.
In such a case, computational bioinformatics algorithms are highly desired, which will provide fast and accurate membrane protein structure predictions.
Computational methods that predict membrane protein structure from sequence can potentially aid structure determination for such difficult target proteins.
Complete determination of a membrane protein structure requires knowledge of the protein position within the lipid bilayer.
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Anyway, regarding the difficulties in analyzing membrane protein structures, alternative techniques that provide structural information, even at medium resolution, were strongly welcomed.
The remarkable gap between the significance of membrane proteins and the limited number of high resolution membrane protein structures is, in part, due to the availability of membrane proteins for structural biology.
However, solving membrane protein structures through the wet-lab experiments is extremely difficult.
In many of the resolved membrane protein structures, individual monomers interact to form higher ordered oligomers.
The reason is that the solved membrane protein structures are much fewer than the soluble proteins, making the training samples difficult to collect.
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